id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-265900-7lj4bfli	Luo, Honglin	Interplay between the virus and the ubiquitin–proteasome system: molecular mechanism of viral pathogenesis	2015-09-29		.txt	text/plain	5051	258	37	Several proteins encoded by DNA tumor viruses, such as the human papillomavirus (HPV) E6 and E7 proteins [14, 15] and the adenovirus E1B55k/E4orf6 proteins [16] , have been shown to induce the assembly of an E3 ligase complex that contains both viral protein and cellular E3 to catalyze the ubiquitination of p53 and subsequent degradation by the proteasome. In addition to its pro-viral function usurped by viruses as discussed above, the UPS-mediated cellular protein degradation may also represent a host defense mechanism against viral infection. ISG15 and the ISGylation conjugation system represent an important host defense mechanism against infection of a broad spectrum of viruses, including Sindbis virus, Viral interaction with the host ubiquitin-proteasome system (UPS): pro-viral and anti-viral function of the UPS in viral pathogenesis. The UPS, including modification of key signaling molecules involved in innate immunity by ubiquitin or ubiquitin-like modifiers (e.g. SUMO and ISG15), represents an important host anti-viral defense mechanism.	./cache/cord-265900-7lj4bfli.txt	./txt/cord-265900-7lj4bfli.txt